4u08

Structure of Leptospira interrogans LRR protein LIC11098

spinqualitylabelsall models 4u08, resolution 1.95Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4u08 is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA, SO4, ZN NonStd Res: MSE Related: 4zth, 4u06, 4uo9 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Pathogenic Leptospira spp. are the agents of leptospirosis, an emerging zoonotic disease. Analyses of Leptospira genomes have shown that the pathogenic leptospires (but not the saprophytes) possess a large number of genes encoding proteins containing leucine-rich repeat (LRR) domains. In other pathogenic bacteria, proteins with LRR domains have been shown to be involved in mediating host-cell attachment and invasion, but their functions remain unknown in Leptospira. To gain insight into the potential function of leptospiral LRR proteins, the crystal structures of four LRR proteins that represent a novel subfamily with consecutive stretches of a 23-amino-acid LRR repeat motif have been solved. The four proteins analyzed adopt the characteristic alpha/beta-solenoid horseshoe fold. The exposed residues of the inner concave surfaces of the solenoid, which constitute a putative functional binding site, are not conserved. The various leptospiral LRR proteins could therefore recognize distinct structural motifs of different host proteins and thus serve separate and complementary functions in the physiology of these bacteria. Structural characterization of a novel subfamily of leucine-rich repeat proteins from the human pathogen Leptospira interrogans.,Miras I, Saul F, Nowakowski M, Weber P, Haouz A, Shepard W, Picardeau M Acta Crystallogr D Biol Crystallogr. 2015 Jun;71(Pt 6):1351-9. doi:, 10.1107/S139900471500704X. Epub 2015 May 23. PMID:26057675 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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